ID A0A061NWG4_9BACL Unreviewed; 697 AA.
AC A0A061NWG4;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00012555};
DE EC=2.4.1.129 {ECO:0000256|ARBA:ARBA00012555};
GN ORFNames=JCM19038_690 {ECO:0000313|EMBL:GAK06976.1};
OS Geomicrobium sp. JCM 19038.
OC Bacteria; Bacillota; Bacilli; Bacillales; Geomicrobium.
OX NCBI_TaxID=1460635 {ECO:0000313|EMBL:GAK06976.1, ECO:0000313|Proteomes:UP000027014};
RN [1] {ECO:0000313|EMBL:GAK06976.1, ECO:0000313|Proteomes:UP000027014}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 19038 {ECO:0000313|EMBL:GAK06976.1,
RC ECO:0000313|Proteomes:UP000027014};
RA Kudo T., Nakahara T., Zhang X., Taniyama S., Arakawa O., Murase S.,
RA Nakata H., Oshima K., Suda W., Kitamura K., Iida T., Oshida Y., Inoue T.,
RA Hongoh Y., Hattori M., Ohkuma M.;
RT "Draft Genome Sequences of Geomicrobium sp. Strains JCM 19037, JCM 19038,
RT JCM 19039, and JCM 19055, Isolated from Aquatic Samples.";
RL Genome Announc. 2:e00622-14(2014).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-
CC Ala)](n)-di-trans,octa-cis-undecaprenyl diphosphate + beta-D-GlcNAc-
CC (1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-di-trans,octa-
CC cis-undecaprenyl diphosphate = [GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-
CC D-Glu-L-Lys-D-Ala-D-Ala)](n+1)-di-trans-octa-cis-undecaprenyl
CC diphosphate + di-trans,octa-cis-undecaprenyl diphosphate + H(+);
CC Xref=Rhea:RHEA:23708, Rhea:RHEA-COMP:9602, Rhea:RHEA-COMP:9603,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:58405, ChEBI:CHEBI:60033,
CC ChEBI:CHEBI:78435; EC=2.4.1.129;
CC Evidence={ECO:0000256|ARBA:ARBA00023988};
CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC {ECO:0000256|ARBA:ARBA00004752}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:GAK06976.1}.
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DR EMBL; BAXA01000002; GAK06976.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A061NWG4; -.
DR eggNOG; COG0744; Bacteria.
DR Proteomes; UP000027014; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0008658; F:penicillin binding; IEA:InterPro.
DR GO; GO:0008955; F:peptidoglycan glycosyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0009002; F:serine-type D-Ala-D-Ala carboxypeptidase activity; IEA:UniProtKB-EC.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 1.10.3810.10; Biosynthetic peptidoglycan transglycosylase-like; 1.
DR Gene3D; 3.40.710.10; DD-peptidase/beta-lactamase superfamily; 1.
DR InterPro; IPR012338; Beta-lactam/transpept-like.
DR InterPro; IPR001264; Glyco_trans_51.
DR InterPro; IPR023346; Lysozyme-like_dom_sf.
DR InterPro; IPR036950; PBP_transglycosylase.
DR InterPro; IPR001460; PCN-bd_Tpept.
DR NCBIfam; TIGR02074; PBP_1a_fam; 1.
DR PANTHER; PTHR32282; BINDING PROTEIN TRANSPEPTIDASE, PUTATIVE-RELATED; 1.
DR PANTHER; PTHR32282:SF11; PENICILLIN-BINDING PROTEIN 1B; 1.
DR Pfam; PF00912; Transgly; 1.
DR Pfam; PF00905; Transpeptidase; 1.
DR SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1.
DR SUPFAM; SSF53955; Lysozyme-like; 1.
PE 4: Predicted;
KW Carboxypeptidase {ECO:0000256|ARBA:ARBA00022645};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000027014};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 20..45
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 64..236
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 328..599
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
SQ SEQUENCE 697 AA; 78672 MW; 554D801A7F3FD6B7 CRC64;
MEVATRRSQR KKRRRFWFRF TFRSTMVIAI LSVLALLCIF SYSYLLGPPP MQVAQSTYIY
DDDGNVVNET QQGHQRNWTN IDDVSPFVLD AFVAIEDRKF YDHHGFDYMR IGAAVLKNVQ
TMSRSQGAST ITQQYARNLF LNHEKTWDRK AREALYALRL EWHVPKDDIL EGYVNTINFG
HGAYGIERAA HLYFGVSAKE LSLEQAALLA GLPRGPSYYS PYNHPERAKD RQELILLRKT
KVKSPLNSTK RHSRLILNSP ETQQSQERVA PYFQDVVERE LLERYDLDPA IVEAGGLKVF
TTLDADLQKA AETYVEQEMP ADEPLQTAVV SVDPTTGDVK AMVGGVHYDE SPFNRAYDAR
RSPGSTFKPF LYYAALKNGF TPATLLRSEP TSFPLNEEGD YYEPGNYGEI YANDFITMTQ
ALAYSDNIYA VKTHVLQEPE SLIETAQAAG IESTLSPNLS LALGASDVGV LELTAAYSPF
ANGGARVEPR LIERVEDAEG NVLIDTEPEV EQAFDERQTY MMTEMMRHMF NSELNDYTSV
TGNSISHLIT RPMAGKSGST PNDNWMIGYT PNLVTGVWVG YDDNTPLDHR KHGQIAKKIW
VKTLEKSLEG ELKHEFQMPP GVENVDIDLA TGLLADEACG NAYTAAFVRN TAPTESCTEY
LENDELNAEE AKEEISKEKE KLFDRLKRWF SSNEIDG
//
